Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): An overview of their mechanisms of formation
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Advanced lipoxidation end products (ALEs) and advanced glycation end products (AGEs) have a pathogenetic role in the development and progression of different oxidative-based diseases including diabetes, atherosclerosis, and neurological disorders. AGEs and ALEs represent a quite complex class of compounds that are formed by different mechanisms, by heterogeneous precursors and that can be formed either exogenously or endogenously. There is a wide interest in AGEs and ALEs involving different aspects of research which are essentially focused on set-up and application of analytical strategies (1) to identify, characterize, and quantify AGEs and ALEs in different pathophysiological conditions; (2) to elucidate the molecular basis of their biological effects; and (3) to discover compounds able to inhibit AGEs/ALEs damaging effects not only as biological tools aimed at validating AGEs/ALEs as drug target, but also as promising drugs. All the above-mentioned research stages require a clear picture of the chemical formation of AGEs/ALEs but this is not simple, due to the complex and heterogeneous pathways, involving different precursors and mechanisms. In view of this intricate scenario, the aim of the present review is to group the main AGEs and ALEs and to describe, for each of them, the precursors and mechanisms of formation.
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4-Hydroxy-2-nonenal (4-HNE) forms stable Michael adducts with cysteine and histidine; nucleophilic attack of lysine forms unstable Michael adducts that require reduction prior to analysis.
“This positive partial charge is attacked by nucleophiles such as cysteine and histidine and stable Michael adducts are formed (Fig. 4B) [50]. Nucleophilic attack of lysine forms unstable Michael adducts, which require reduction, e.g., by sodium borohydride prior to analysis [57].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [50]
Cites
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672 · see citing works
Rio, D. D., Stewart, A. J., & Pellegrini, N. (2005) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2005.05.003 · Cited by 2,733 · see citing works
Advanced glycation end-products: A review
Singh, R., Barden, A., Mori, T., & Beilin, L. (2001) · Diabetologia · doi:10.1007/s001250051591 · Cited by 2,597 · see citing works
Isolation and characterization
Turksen, K. (2006) · Humana Press eBooks · Cited by 2,082 · see citing works
Dehydrated Foods, Chemistry of Browning Reactions in Model Systems
Hodge, J. E. (1953) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60015a004 · Cited by 1,950 · see citing works
Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
Thornalley, P. J., LANGBORG, A., & Minhas, H. S. (1999) · Biochemical Journal · doi:10.1042/bj3440109 · Cited by 1,209 · see citing works
Lipid peroxidation: Physiological levels and dual biological effects
Niki, E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.032 · Cited by 1,006 · see citing works
The Role of Advanced Glycation End Products in Progression and Complications of Diabetes
Goh, S.-Y., & Cooper, M. E. (2008) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2007-1817 · Cited by 987 · see citing works
Ramasamy, R., Vannucci, S. J., Yan, S. S. D., Herold, K., Yan, S. F., & Schmidt, A. M. (2005) · Glycobiology · doi:10.1093/glycob/cwi053 · Cited by 834 · see citing works
Fu, M.-X., Requena, J. R., Jenkins, A. J., Lyons, T. J., Baynes, J. W., & Thorpe, S. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.9982 · Cited by 822 · see citing works
Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily
Marchitti, S. A., Brocker, C. N., Stagos, D., & Vasiliou, V. (2008) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.4.6.697 · Cited by 806 · see citing works
Large-scale fluid/fluid phase separation of proteins and lipids in giant plasma membrane vesicles
Baumgart, T., Hammond, A. T., Sengupta, P., Hess, S. T., Holowka, D. A., Baird, B. A., & Webb, W. W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611357104 · Cited by 801 · see citing works
Nonenzymatic Browning in Vivo: Possible Process for Aging of Long-Lived Proteins
Monnier, V. M., & Cerami, A. (1981) · Science · doi:10.1126/science.6779377 · Cited by 768 · see citing works
Acrolein: Sources, metabolism, and biomolecular interactions relevant to human health and disease
Stevens, J. F., & Maier, C. S. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700412 · Cited by 756 · see citing works
Fu, T., Jacob, D. J., Wittrock, F., Burrows, J. P., Vrekoussis, M., & Henze, D. K. (2008) · Journal of Geophysical Research Atmospheres · doi:10.1029/2007jd009505 · Cited by 746 · see citing works
Aldehyde Sources, Metabolism, Molecular Toxicity Mechanisms, and Possible Effects on Human Health
O'Brien, P. J., Siraki, A. G., & Shangari, N. (2005) · Critical Reviews in Toxicology · doi:10.1080/10408440591002183 · Cited by 738 · see citing works
Melanoidins produced by the Maillard reaction: Structure and biological activity
Wang, H.-Y., Qian, H., & Yao, W.-R. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.03.075 · Cited by 719 · see citing works
Lo, T. W. C., Westwood, M. E., McLellan, A. C., Selwood, T., & Thornalley, P. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31635-1 · Cited by 695 · see citing works
Choudhary, V., Mushrif, S. H., Ho, C. R., Anderko, A., Nikolakis, V. A., Marinković, N., Frenkel, A. I., Sandler, S. I., & Vlachos, D. G. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3122763 · Cited by 685 · see citing works
Negre‐Salvayre, A., Coatrieux, C., Ingueneau, C., & Salvayre, R. (2008) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707395 · Cited by 641 · see citing works
Generation and Biological Activities of Oxidized Phospholipids
Bochkov, V. N., Oskolkova, O., Birukov, K. G., Levonen, A., Binder, C. J., & Stöckl, J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2597 · Cited by 611 · see citing works
Ahmed, M. U., Frye, E. B., Degenhardt, T. P., Thorpe, S. R., & Baynes, J. (1997) · Biochemical Journal · doi:10.1042/bj3240565 · Cited by 605 · see citing works
Reaction of Monosaccharides with Proteins: Possible Evolutionary Significance
Bunn, H. F., & Higgins, P. J. (1981) · Science · doi:10.1126/science.12192669 · Cited by 598 · see citing works
Wells‐Knecht, K. J., Zyzak, D. V., Litchfield, J., Thorpe, S. R., & Baynes, J. (1995) · Biochemistry · doi:10.1021/bi00011a027 · Cited by 594 · see citing works
Thornalley, P. J. (1996) · General Pharmacology: The Vascular System · doi:10.1016/0306-3623(95)02054-3 · Cited by 591 · see citing works
Action des acides amines sur les sucres : formation des melanoidines par voie methodique
Maillard, L. (1912) · Medical Entomology and Zoology · Cited by 574 · see citing works
Chemistry and biochemistry of lipid peroxidation products
Guéraud, F., Atalay, M., Bresgen, N., Gašparović, A. Č., Eckl, P., Laurence Therese, H. U. C., Jouanin, I., Siems, W., & Uchida, K. (2010) · Free Radical Research · doi:10.3109/10715762.2010.498477 · Cited by 556 · see citing works
Dyer, D. G., Blackledge, J. A., Thorpe, S. R., & Baynes, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99007-1 · Cited by 535 · see citing works
Uchida, K., & Stadtman, E. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53264-6 · Cited by 513 · see citing works
Methylglyoxal in living organisms
Kalapos, M. P. (1999) · Toxicology Letters · doi:10.1016/s0378-4274(99)00160-5 · Cited by 507 · see citing works
The Chemistry and Technology of Furfural and its Many By-products
Li, J. Q. (2001) · Chemical Engineering Journal · doi:10.1016/s1385-8947(00)00182-0 · Cited by 498 · see citing works
The use of ozone and associated oxidation processes in drinking water treatment
Camel, V., & Bermond, A. (1998) · Water Research · doi:10.1016/s0043-1354(98)00130-4 · Cited by 465 · see citing works
Grandhee, S. K., & Monnier, V. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99006-x · Cited by 459 · see citing works
4-Hydroxynonenal as a bioactive marker of pathophysiological processes
Žarković, N. (2003) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(03)00023-2 · Cited by 398 · see citing works
Dietary Advanced Glycation End Products and Aging
Luevano-Contreras, C., & Chapman-Novakofski, K. (2010) · Nutrients · doi:10.3390/nu2121247 · Cited by 396 · see citing works
15-Deoxy-Δ12,14-prostaglandin J2
Shibata, T., Kondo, M., Osawa, T., Shibata, N., Kobayashi, M., & Uchida, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110314200 · Cited by 391 · see citing works
Thornalley, P. J. (1998) · PubMed · Cited by 387 · see citing works
Pamplona, R. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.07.003 · Cited by 387 · see citing works
New Hemoglobin in Normal Adult Blood
Kunkel, H. G., & Wallenius, G. (1955) · Science · doi:10.1126/science.122.3163.288 · Cited by 377 · see citing works
Methylglyoxal Modification of Protein
Oya, T., Hattori, N., Mizuno, Y., Miyata, S., Maeda, S., Osawa, T., & Uchida, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.26.18492 · Cited by 374 · see citing works
Protein Adducts Generated from Products of Lipid Oxidation: Focus on HNE and ONE
Sayre, L. M., Lin, D., Yuan, Q., Zhu, X., & Tang, X. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600959508 · Cited by 364 · see citing works
1,2-Dicarbonyl Compounds in Commonly Consumed Foods
Degen, J., Hellwig, M., & Henle, T. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf301306g · Cited by 360 · see citing works
the chemistry and technology of furfural and its many by-products
(2000) · Sugar series · doi:10.1016/s0167-7675(00)x8001-3 · Cited by 351 · see citing works
Toxicology and risk assessment of 5‐Hydroxymethylfurfural in food
Abraham, K., Gürtler, R., Berg, K., Heinemeyer, G., Lampen, A., & Appel, K. E. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201000564 · Cited by 340 · see citing works
Application of the Hard and Soft, Acids and Bases (HSAB) Theory to Toxicant–Target Interactions
LoPachin, R. M., Gavin, T., DeCaprio, A. P., & Barber, D. S. (2011) · Chemical Research in Toxicology · doi:10.1021/tx2003257 · Cited by 327 · see citing works
Advanced glycation end products and neurodegenerative diseases: Mechanisms and perspective
Li, J., Liu, D., Sun, L., Lu, Y., & Zhang, Z. (2012) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2012.02.018 · Cited by 320 · see citing works
The importance of lipid-derived malondialdehyde in diabetes mellitus
Slatter, D. A., Bolton, C., & Bailey, A. J. (2000) · Diabetologia · doi:10.1007/s001250051342 · Cited by 318 · see citing works
Protein Cross-linking by the Maillard Reaction
Nagaraj, R. H., Shipanova, I. N., & Faust, F. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.32.19338 · Cited by 304 · see citing works
Current Status of Acrolein as a Lipid Peroxidation Product
Uchida, K. (1999) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(99)00016-x · Cited by 299 · see citing works
Yamagishi, S., Maeda, S., Matsui, T., Ueda, S., Fukami, K., & Okuda, S. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.03.014 · Cited by 297 · see citing works
Huber, J., Vales, A., Mitulović, G., Blumer, M. J. F., Schmid, R., Witztum, J. L., Binder, B. R., & Leitinger, N. (2002) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0102.101525 · Cited by 296 · see citing works
Intervention strategies to inhibit protein carbonylation by lipoxidation‐derived reactive carbonyls
Aldini, G., Dalle‐Donne, I., Facino, R. M., Milzani, A., & Carini, M. (2006) · Medicinal Research Reviews · doi:10.1002/med.20073 · Cited by 289 · see citing works
Self-citationNürsten, H. E. (2005) · Royal Society of Chemistry eBooks · doi:10.1039/9781847552570 · Cited by 284 · see citing works
Kinetic study on the Maillard reaction. Consideration of sugar reactivity
Laroque, D., Inisan, C., Berger, C., Vouland, É., Dufossé, L., & Guérard, F. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2008.05.033 · Cited by 283 · see citing works
Molecular Basis of Arterial Stiffening: Role of Glycation – A Mini-Review
Sell, D. R., & Monnier, V. M. (2012) · Gerontology · doi:10.1159/000334668 · Cited by 281 · see citing works
Shipanova, I. N., Glomb, M. A., & Nagaraj, R. H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0195 · Cited by 279 · see citing works
Routes to 4-Hydroxynonenal: Fundamental Issues in the Mechanisms of Lipid Peroxidation
Schneider, C. G., Porter, N. A., & BRASH, A. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800001200 · Cited by 275 · see citing works
Mechanism for the formation of methylglyoxal from triosephosphates
Richard, J. P. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210549 · Cited by 272 · see citing works
LoPachin, R. M., Gavin, T., Petersen, D. R., & Barber, D. S. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900147g · Cited by 263 · see citing works
Erbersdobler, H. F., & Somoza, V. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200600154 · Cited by 261 · see citing works
The metabolism of acetone in rat.
Casazza, J. P., Felver, M., & Veech, R. L. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43646-5 · Cited by 260 · see citing works
Jagt, D. L. V., & Hunsaker, L. A. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00212-0 · Cited by 256 · see citing works
The tandem of free radicals and methylglyoxal
Kalapos, M. P. (2007) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2007.11.009 · Cited by 252 · see citing works
METABOLISM OF METHYLGLYOXAL IN MICROORGANISMS
Cooper, R. A. (1984) · Annual Review of Microbiology · doi:10.1146/annurev.mi.38.100184.000405 · Cited by 252 · see citing works
Physiological relevance of dietary melanoidins
Morales, F. J., Somoza, V., & Fogliano, V. (2010) · Amino Acids · doi:10.1007/s00726-010-0774-1 · Cited by 248 · see citing works
Nonenzymatic Glycation of Bovine Serum Albumin by Fructose (Fructation)
Suárez, G., Rajaram, R., Oronsky, A. L., & Gawinowicz, M. A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84904-9 · Cited by 244 · see citing works
Characterization of 4-Oxo-2-nonenal as a Novel Product of Lipid Peroxidation
Lee, S. H., & Blair, I. A. (2000) · Chemical Research in Toxicology · doi:10.1021/tx000101a · Cited by 244 · see citing works
Chemical modification of proteins by methylglyoxal.
Degenhardt, T. P., Thorpe, S. R., & Baynes, J. (1998) · PubMed · Cited by 243 · see citing works
Mutarotation, Hydrolysis, and Rearrangement Reactions of Glycosylamines1
Isbell, H. S., & Frush, H. L. (1958) · The Journal of Organic Chemistry · doi:10.1021/jo01103a019 · Cited by 237 · see citing works
Seiler, N. (2004) · Amino Acids · doi:10.1007/s00726-004-0070-z · Cited by 236 · see citing works
Structural Definition of Early Lysine and Histidine Adduction Chemistry of 4-Hydroxynonenal
Nadkarni, D. V., & Sayre, L. M. (1995) · Chemical Research in Toxicology · doi:10.1021/tx00044a014 · Cited by 235 · see citing works
Flavour chemistry of methylglyoxal and glyoxal
Wang, Y., & Ho, C. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35025d · Cited by 230 · see citing works
Insights into Oxidative Stress: The Isoprostanes
Montuschi, P., Barnes, P. J., & Roberts, L. J. (2007) · Current Medicinal Chemistry · doi:10.2174/092986707780059607 · Cited by 230 · see citing works
Lyles, G. A. (1996) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/1357-2725(95)00130-1 · Cited by 228 · see citing works
Westwood, M. E., & Thornalley, P. J. (1995) · Journal of Protein Chemistry · doi:10.1007/bf01886793 · Cited by 227 · see citing works
The Maillard reaction in the human body. The main discoveries and factors that affect glycation
Tessier, F. J. (2009) · Pathologie Biologie · doi:10.1016/j.patbio.2009.09.014 · Cited by 222 · see citing works
The road to advanced glycation end products: a mechanistic perspective
Cho, S.-J., Roman, G., Yeboah, F., & Konishi, Y. (2007) · Current Medicinal Chemistry · doi:10.2174/092986707780830989 · Cited by 213 · see citing works
Glucosepane Is a Major Protein Cross-link of the Senescent Human Extracellular Matrix
Sell, D. R., Biemel, K. M., Reihl, O., Lederer, M. O., Strauch, C., & Monnier, V. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500733200 · Cited by 212 · see citing works
Biemel, K. M., Friedl, D. A., & Lederer, M. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202681200 · Cited by 210 · see citing works
Bein, K., & Leikauf, G. D. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100279 · Cited by 210 · see citing works
A Comparative Review of Petroleum‐Based and Bio‐Based Acrolein Production
Liu, L., Ye, X. P., & Bozell, J. J. (2012) · ChemSusChem · doi:10.1002/cssc.201100447 · Cited by 210 · see citing works
Fructose-mediated non-enzymatic glycation: sweet coupling or bad modification
Schalkwijk, C. G., Stehouwer, C. D. A., & van Hinsbergh, V. W. M. (2004) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.488 · Cited by 206 · see citing works
Aldehydic lipid peroxidation products derived from linoleic acid
Spiteller, P. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(01)00100-7 · Cited by 201 · see citing works
Advanced lipoxidation end-products
Pamplona, R. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.01.007 · Cited by 200 · see citing works
Sugars as tobacco ingredient: Effects on mainstream smoke composition
Talhout, R., Opperhuizen, A., & van Amsterdam, J. (2006) · Food and Chemical Toxicology · doi:10.1016/j.fct.2006.06.016 · Cited by 199 · see citing works
Determination of toxic carbonyl compounds in cigarette smoke
Fujioka, K., & Shibamoto, T. (2006) · Environmental Toxicology · doi:10.1002/tox.20153 · Cited by 197 · see citing works
Rippe, J. M., & Angelopoulos, T. J. (2013) · Advances in Nutrition · doi:10.3945/an.112.002824 · Cited by 194 · see citing works
Structure and Mechanism of Formation of Human Lens Fluorophore LM-1
Tessier, F. J., Obrenovich, M. E., & Monnier, V. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.20796 · Cited by 188 · see citing works
Oxidatively modified autoantigens in autoimmune diseases
Kurien, B. T., Hensley, K., Bachmann, M. P., & Scofield, R. H. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.05.020 · Cited by 186 · see citing works
AGEs in foods: do they play a role in uremia?
Henle, T. (2003) · Kidney International · doi:10.1046/j.1523-1755.63.s84.16.x · Cited by 184 · see citing works
Trans-4-hydroxy-2-hexenal, a product of n-3 fatty acid peroxidation: Make some room HNE…
Long, E. K., & Picklo, M. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.015 · Cited by 178 · see citing works
New Insights Regarding the Autoxidation of Polyunsaturated Fatty Acids
Yin, H., & Porter, N. A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.170 · Cited by 177 · see citing works
Degradation of Glucose: Reinvestigation of Reactive α-Dicarbonyl Compounds †
Gobert, J., & Glomb, M. A. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9019085 · Cited by 175 · see citing works
The cytotoxic mechanism of glyoxal involves oxidative stress
Shangari, N., & O’Brien, P. J. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.06.013 · Cited by 174 · see citing works
Effects of Smoking Cessation on Eight Urinary Tobacco Carcinogen and Toxicant Biomarkers
Carmella, S. G., Chen, M., Han, S., Briggs, A., Jensen, J., Hatsukami, D. K., & Hecht, S. S. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800479s · Cited by 174 · see citing works
Protein fructosylation: fructose and the Maillard reaction
Dills, W. (1993) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/58.5.779s · Cited by 171 · see citing works
Toxicology and risk assessment of acrolein in food
Abraham, K., Andres, S., Palavinskas, R., Berg, K., Appel, K. E., & Lampen, A. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100481 · Cited by 170 · see citing works
Hamada, Y., Araki, N., Koh, N., Nakamura, J., Horiuchi, S., & Hotta, N. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1695 · Cited by 169 · see citing works
4-Oxo-2-nonenal Is Both More Neurotoxic and More Protein Reactive than 4-Hydroxy-2-nonenal
Lin, D., Lee, H., Liu, Q., Perry, G. L., Smith, M. A., & Sayre, L. M. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050080q · Cited by 164 · see citing works
An update on advanced glycation endproducts and atherosclerosis
Turco, S. D., & Basta, G. (2012) · BioFactors · doi:10.1002/biof.1018 · Cited by 156 · see citing works
Zeng, J., & Davies, M. J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050074u · Cited by 153 · see citing works
The pathogenic role of Maillard reaction in the aging eye
Nagaraj, R. H., Linetsky, M. D., & Stitt, A. W. (2010) · Amino Acids · doi:10.1007/s00726-010-0778-x · Cited by 151 · see citing works
Karachalias, N., Babaei‐Jadidi, R., Ahmed, N., & Thornalley, P. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311423 · Cited by 150 · see citing works
Advanced Glycation End Products and Diabetic Cardiovascular Disease
Prasad, A., Bekker, P., & Tsimikas, S. (2012) · Cardiology in Review · doi:10.1097/crd.0b013e318244e57c · Cited by 150 · see citing works
Dietary advanced glycation endproducts (AGEs) and their health effects – PRO
Šebeková, K., & Somoza, V. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700035 · Cited by 148 · see citing works
Covalent adduction of nucleophilic amino acids by 4-hydroxynonenal and 4-oxononenal
Doorn, J. A., & Petersen, D. R. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00178-3 · Cited by 147 · see citing works
Lederer, M. O., & Klaiber, R. (1999) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(99)00212-6 · Cited by 146 · see citing works
3-Deoxyglucosone: metabolism, analysis, biological activity, and clinical implication
Niwa, T. (1999) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(99)00113-9 · Cited by 144 · see citing works
Amides Are Novel Protein Modifications Formed by Physiological Sugars
Glomb, M. A., & Pfahler, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103557200 · Cited by 144 · see citing works
Glycation research in amino acids: a place to call home
Rabbani, N., & Thornalley, P. J. (2010) · Amino Acids · doi:10.1007/s00726-010-0782-1 · Cited by 144 · see citing works
Fate of 4-hydroxynonenal in vivo: disposition and metabolic pathways
Alary, J., Guéraud, F., & Cravedi, J. (2003) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(03)00012-8 · Cited by 143 · see citing works
Lindén, T., Cohen, A. S., Deppisch, R. M., Kjellstrand, P. T. T., & Wieslander, A. P. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00490.x · Cited by 143 · see citing works
Biemel, K. M., Reihl, O., Conrad, J., & Lederer, M. O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102035200 · Cited by 141 · see citing works
Formation of Crossline as a Fluorescent Advanced Glycation End Productin Vitroandin Vivo
Obayashi, H., Nakano, K., Shigeta, H., Yamaguchi, M., Yoshimori, K., Fukui, M., Fujii, M., Kitagawa, Y., Nakamura, N., Nakamura, K., et al. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1308 · Cited by 137 · see citing works
The naturally occurring furanones: formation and function from pheromone to food
Slaughter, J. C. (1999) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1017/s0006323199005332 · Cited by 135 · see citing works
Eisner, B. H., Porten, S. P., Bechis, S. K., & Stoller, M. L. (2010) · The Journal of Urology · doi:10.1016/j.juro.2010.02.007 · Cited by 129 · see citing works
Sell, D. R., Strauch, C., Shen, W., & Monnier, V. M. (2007) · Biochemical Journal · doi:10.1042/bj20061645 · Cited by 126 · see citing works
Butterfield, D. A., Reed, T. T., & Rukhsana Sultana, A. (2010) · Free Radical Research · doi:10.3109/10715762.2010.520014 · Cited by 123 · see citing works
Nakamura, K., Nakazawa, Y., & Ienaga, K. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6262 · Cited by 122 · see citing works
α-Oxoaldehyde metabolism and diabetic complications
Beisswenger, P. J., Howell, S. K., Nelson, R. G., Mauer, M. S., & Szwergold, B. S. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311358 · Cited by 121 · see citing works
Hollnagel, A., & Kroh, L. W. (1998) · Zeitschrift für Lebensmittel-Untersuchung und -Forschung. B, Referate und Lebensmittelrecht · doi:10.1007/s002170050294 · Cited by 120 · see citing works
A New Mechanism of the Maillard Reaction Involving Sugar Fragmentation and Free Radical Formation
Namiki, M., & Hayashi, T. (1983) · ACS symposium series · doi:10.1021/bk-1983-0215.ch002 · Cited by 117 · see citing works
Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes
Delpierre, G., Collard, F., Fortpied, J., & SCHAFTINGEN, E. V. (2002) · Biochemical Journal · doi:10.1042/bj20020325 · Cited by 115 · see citing works
A synopsis of the process of lipid peroxidation since the discovery of the essential fatty acids
Catalá, Á. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.07.087 · Cited by 115 · see citing works
Davídek, T., Robert, F., Devaud, S., Vera, F. A., & Blank, I. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf060668i · Cited by 113 · see citing works
Nϵ-(3-Methylpyridinium)lysine, a Major Antigenic Adduct Generated in Acrolein-modified Protein
Furuhata, A., Ishii, T., Kumazawa, S., Yamada, T., Nakayama, T., & Uchida, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309401200 · Cited by 112 · see citing works
Isolation and Characterization of Glyoxal−Arginine Modifications
Glomb, M. A., & Lang, G. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf001082d · Cited by 109 · see citing works
Henle, T., Walter, A. W., Hae�ner, R., & Klostermeyer, H. (1994) · European Food Research and Technology · doi:10.1007/bf01192954 · Cited by 107 · see citing works
Model Studies on Protein Side Chain Modification by 4-Oxo-2-nonenal
Zhang, W., Liu, J., Xu, G., Yuan, Q., & Sayre, L. M. (2003) · Chemical Research in Toxicology · doi:10.1021/tx020105a · Cited by 107 · see citing works
Thornalley, P. J. (1995) · Critical Reviews in Oncology/Hematology · doi:10.1016/1040-8428(94)00149-n · Cited by 106 · see citing works
Detection and quantification of pentosidine in foods
Henle, T., Schwarzenbolz, U., & Klostermeyer, H. (1997) · Zeitschrift für Lebensmittel-Untersuchung und -Forschung. B, Referate und Lebensmittelrecht · doi:10.1007/s002170050043 · Cited by 104 · see citing works
METHYLGLYOXAL, DIABETES MELLITUS AND DIABETIC COMPLICATIONS
Jagt, D. L. V. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.93 · Cited by 104 · see citing works
Liu, Z., Minkler, P. E., & Sayre, L. M. (2003) · Chemical Research in Toxicology · doi:10.1021/tx0300030 · Cited by 102 · see citing works
Chemical Modifications of Peptides and Their Impact on Food Properties
Lancker, F. V., Adams, A., & KIMPE, N. D. (2011) · Chemical Reviews · doi:10.1021/cr200032j · Cited by 102 · see citing works
Interactions of glutathione transferases with 4-hydroxynonenal
Balogh, L. M., & Atkins, W. M. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.558092 · Cited by 100 · see citing works
Glyoxal Formation and Its Role in Endogenous Oxalate Synthesis
Lange, J. N., Wood, K. D., Knight, J. L., Assimos, D. G., & Holmes, R. P. (2012) · Advances in Urology · doi:10.1155/2012/819202 · Cited by 97 · see citing works
Slatter, D. A., Murray, M., & Bailey, A. J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(97)01554-8 · Cited by 95 · see citing works
Takeuchi, M., Takino, J.-I., & Yamagishi, S. (2010) · Current Drug Targets · doi:10.2174/1389450111009011468 · Cited by 95 · see citing works
Toxicity of glyoxals – role of oxidative stress, metabolic detoxification and thiamine deficiency
Shangari, N., Bruce, W. R., Poon, R. W. M., & O'Brien, P. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311390 · Cited by 94 · see citing works
Acetone catabolism by cytochrome P450 2E1: studies with CYP2E1-null mice
Bondoc, F. Y., Bao, Z., Hu, W., Gonzalez, F. J., Wang, Y., Yang, C. S., & Hong, J. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00111-2 · Cited by 94 · see citing works
3‐Deoxy‐glucosone is an Intermediate in the Formation of Furfurals from D ‐Glucose.
Jadhav, H. S., Pedersen, C. M., Sølling, T. I., & Bols, M. (2011) · ChemSusChem · doi:10.1002/cssc.201100249 · Cited by 94 · see citing works
METHYLGLYOXAL AND GLUCOSE METABOLISM: A HISTORICAL PERSPECTIVE AND FUTURE AVENUES FOR RESEARCH
Kalapos, M. P. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.69 · Cited by 92 · see citing works
Hoff, H. F., O'NEIL, J. A., Wu, Z., Hoppe, G., & Salomon, R. G. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000051407.42536.73 · Cited by 85 · see citing works
Experimental studies on the role of fructose in the development of diabetic complications.
Sakai, M., Oimomi, M., & Kasuga, M. (2002) · PubMed · doi:10.24546/00318725 · Cited by 83 · see citing works
Methylglyoxal production in vascular smooth muscle cells from different metabolic precursors
Dhar, A., Desai, K. M., Kazachmov, M., Yu, P. H., & Wu, L. (2008) · Metabolism · doi:10.1016/j.metabol.2008.04.014 · Cited by 83 · see citing works
The role of dicarbonyl compounds in non-enzymatic crosslinking: a structure–activity study
Meade, S. J., Miller, A. G., & Gerrard, J. A. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(02)00564-3 · Cited by 79 · see citing works
Reactions of Lipid-derived Malondialdehyde with Collagen
Slatter, D. A., Paul, R. G., Murray, M., & Bailey, A. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19661 · Cited by 78 · see citing works
Chemical Modification of Proteins by Lipids in Diabetes
Baynes, J. (2003) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2003.179 · Cited by 77 · see citing works
Iacobini, C., Menini, S., Ricci, P. C., Scipioni, A., Sansoni, V., Mazzitelli, G., Cordone, S., Pesce, C. M., Pugliese, F. R., Pricci, F., et al. (2009) · The Journal of Pathology · doi:10.1002/path.2536 · Cited by 76 · see citing works
Gensberger‐Reigl, S., Mittelmaier, S., Glomb, M. A., & Pischetsrieder, M. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-5817-x · Cited by 75 · see citing works
MOLECULAR ENZYMOLOGY OF THE GLYOXALASE SYSTEM
Mannervik, B. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.13 · Cited by 74 · see citing works
Structure of advanced Maillard reaction products and their pathological role
Monnier, V. M., Nagaraj, R. H., Portero‐Otín, M., Glomb, M. A., Elgawish, A.-H., Sell, D. R., & Friedlander, M. A. (1996) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/11.supp5.20 · Cited by 74 · see citing works
Iijima, K., Murata, M., Takahara, H., Irie, S., & Fujimoto, D. (2000) · Biochemical Journal · doi:10.1042/bj3470023 · Cited by 74 · see citing works
Slatter, D. A., Avery, N. C., & Bailey, A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310608200 · Cited by 73 · see citing works
Minor Strecker degradation products of phenylalanine and phenylglycine
Adamiec, J., Rössner, J., Velı́šek, J., Cejpek, K., & ŠAVEL, J. (2001) · European Food Research and Technology · doi:10.1007/s002170000234 · Cited by 73 · see citing works
Klöpfer, A., Spanneberg, R., & Glomb, M. A. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf103116c · Cited by 73 · see citing works
Production of 1,2-Propanediol from Glycerol in Saccharomyces cerevisiae
Jung, J. Y. (2011) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1103.03009 · Cited by 70 · see citing works
Fan, X., Sell, D. R., Zhang, J., Nemet, I., Theves, M., Lu, J., Strauch, C., Halushka, M. K., & Monnier, V. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.06.003 · Cited by 70 · see citing works
Iijima, K., Murata, M., Takahara, H., et al. (2000) · PubMed · Cited by 69 · see citing works
Cui, Q., & Karplus, M. (2003) · Advances in protein chemistry · doi:10.1016/s0065-3233(03)66008-0 · Cited by 68 · see citing works
Raman spectroscopy of glyoxal oligomers in aqueous solutions
Avzianova, E., & Brooks, S. D. (2012) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2012.09.050 · Cited by 68 · see citing works
Isoketals: highly reactive γ-ketoaldehydes formed from the H2-isoprostane pathway
Davies, S. S., Amarnath, V., & Roberts, L. J. (2003) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2003.10.007 · Cited by 67 · see citing works
Mass Spectroscopic Characterization of Protein Modification by Malondialdehyde
Ishii, T., Kumazawa, S., Sakurai, T., Nakayama, T., & Uchida, K. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050231p · Cited by 66 · see citing works
Sell, D. R., & Monnier, V. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408946200 · Cited by 65 · see citing works
Increased erythrocyte 3-DG and AGEs in diabetic hemodialysis patients: Role of the polyol pathway
Tsukushi, S., Katsuzaki, T., Aoyama, I., Takayama, F., Miyazaki, T., Shimokata, K., & Niwa, T. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.00418.x · Cited by 63 · see citing works
Identification and Determination of α-Dicarbonyl Compounds Formed in the Degradation of Sugars
Usui, T., Yanagisawa, S., OHGUCHI, M., YOSHINO, M., Kawabata, R., KISHIMOTO, J., Arai, Y., Kaoru, A. I. D. A., Watanabe, H., & Hayase, F. (2007) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70229 · Cited by 60 · see citing works
Chemistry and biochemistry of lipid peroxidation products. Free Radic Res
Guéraud, F., Atalay, M., Bresgen, N., et al. (2010) · Cited by 60 · see citing works
On the reaction of glyoxal with proteins
Schwarzenbolz, U., Henle, T., Haeßner, R., & Klostermeyer, H. (1997) · Zeitschrift für Lebensmittel-Untersuchung und -Forschung. B, Referate und Lebensmittelrecht · doi:10.1007/s002170050137 · Cited by 59 · see citing works
Geißler, S., Hellwig, M., Zwarg, M., Markwárdt, F., Henle, T., & Brandsch, M. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903791u · Cited by 59 · see citing works
Nagaraj, R. H., Portero‐Otín, M., & Monnier, V. M. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0019 · Cited by 58 · see citing works
α‐Dicarbonyl Compounds—Key Intermediates for the Formation of Carbohydrate‐based Melanoidins
Kroh, L. W., Fiedler, T., & Wagner, J. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1433.058 · Cited by 58 · see citing works
Kuiper, H. C., Miranda, C. L., Sowell, J. D., & Stevens, J. F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802797200 · Cited by 57 · see citing works
Nonenzymatic browning reactions of retro-aldol degradation products of carbohydrates
Cämmerer, B., Wedzicha, B. L., & Kroh, L. W. (1999) · European Food Research and Technology · doi:10.1007/s002170050490 · Cited by 57 · see citing works
The dual face of endogenous α-aminoketones: Pro-oxidizing metabolic weapons
Bechara, E. J. H., Dutra, F., Cardoso, V. E. S., Sartori, A., Olympio, K. P. K., Penatti, C. A. A., Adhikari, A., & Assunção, N. A. (2007) · Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology · doi:10.1016/j.cbpc.2006.07.004 · Cited by 57 · see citing works
Niwa, T., Katsuzaki, T., Ishizaki, Y., Hayase, F., Miyazaki, T., Uematsu, T., Tatemichi, N., & Takei, Y. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00362-1 · Cited by 56 · see citing works
Niwa, H., Takeda, A., Wakai, M., Miyata, T., Yasuda, Y., Mitsuma, T., Kurokawa, K., & Sobue, G. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8899 · Cited by 56 · see citing works
3-Deoxyfructose Concentrations are Increased in Human Plasma and Urine in Diabetes
Wells‐Knecht, K. J., Lyons, T. J., McCance, D. R., Thorpe, S. R., Feather, M. S., & Baynes, J. (1994) · Diabetes · doi:10.2337/diab.43.9.1152 · Cited by 55 · see citing works
Nakayama, T., Hayase, F., & Kato, H. (1980) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.44.1201 · Cited by 54 · see citing works
Glyoxal formation by Fenton-induced degradation of carbohydrates and related compounds
Manini, P., Pietra, P. L., Panzella, L., Napolitano, A., & d’Ischia, M. (2006) · Carbohydrate Research · doi:10.1016/j.carres.2006.03.027 · Cited by 53 · see citing works
Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease
Cotham, W. E., Metz, T., Ferguson, P. L., Brock, J. W. C., Hinton, D. J. S., Thorpe, S. R., Baynes, J., & Ames, J. M. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400002-mcp200 · Cited by 53 · see citing works
Jono, T. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh124 · Cited by 51 · see citing works
Cooper, R. A. (1975) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(75)41106-5 · Cited by 50 · see citing works
Muñoz‐Clares, R. A., Díaz‐Sánchez, Á. G., González‐Segura, L., & Montiel, C. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.09.006 · Cited by 48 · see citing works
Wang, Y., & Ho, C. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf8012025 · Cited by 48 · see citing works
Yang, K., Dong, Q., Delaney, S., Mehta, R., Bruce, W. R., & O’Brien, P. J. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.02.012 · Cited by 48 · see citing works
Modulation of Insulin Action by Advanced Glycation Endproducts: A New Player in the Field
Schalkwijk, C. G., Brouwers, O., & Stehouwer, C. D. A. (2008) · Hormone and Metabolic Research · doi:10.1055/s-0028-1082085 · Cited by 47 · see citing works
Maeshima, T., Honda, K., Chikazawa, M., Shibata, T., Kawai, Y., Akagawa, M., & Uchida, K. (2012) · Chemical Research in Toxicology · doi:10.1021/tx3000818 · Cited by 47 · see citing works
Wang, T., Kartika, R., & Spiegel, D. A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja301994d · Cited by 47 · see citing works
Elevated level of methylglyoxal during diabetic ketoacidosis and its recovery phase
Turk, Z., Nemet, I., Varga‐Defterdarovič, L., & Car, N. (2006) · Diabetes & Metabolism · doi:10.1016/s1262-3636(07)70266-5 · Cited by 47 · see citing works
Methylglyoxal determination from different carbohydrates during heat processing
Homoki-Farkas, P., Örsi, F., & Kroh, L. W. (1997) · Food Chemistry · doi:10.1016/s0308-8146(96)00273-7 · Cited by 46 · see citing works
Site-specific modification of positively-charged surfaces on human serum albumin by malondialdehyde
Ishii, T., Ito, S., Kumazawa, S., Sakurai, T., Yamaguchi, S., Mori, T., Nakayama, T., & Uchida, K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.140 · Cited by 46 · see citing works
In vitro production of long chain pyrrole fatty esters from carbonyl-amine reactions.
Hidalgo, F. J., & Zamora, R. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)40058-6 · Cited by 46 · see citing works
Chapter 31 Some aspects of the pathophysiology of semicarbazide-sensitive amine oxidase enzymes
Callingham, B. A., Crosbie, A. E., & Rous, B. (1995) · Progress in brain research · doi:10.1016/s0079-6123(08)61227-3 · Cited by 45 · see citing works
Noda, Y., & Peterson, D. G. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf063423e · Cited by 45 · see citing works
Hayase, F., Konishi, Y., & Kato, H. (1995) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.59.1407 · Cited by 45 · see citing works
Aldose Reductase, Oxidative Stress and Diabetic Cardiovascular Complications
Vedantham, S., Ananthakrishnan, R., Schmidt, A. M., & Ramasamy, R. (2012) · Cardiovascular & Hematological Agents in Medicinal Chemistry · doi:10.2174/187152512802651097 · Cited by 45 · see citing works
Reactivity of Thermally Treated α-Dicarbonyl Compounds
Pfeifer, Y. V., Haase, P. T., & Kroh, L. W. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf302959k · Cited by 45 · see citing works
Collard, F., Vertommen, D., Fortpied, J., Duester, G., & SCHAFTINGEN, E. V. (2006) · Biochimie · doi:10.1016/j.biochi.2006.11.005 · Cited by 42 · see citing works
Arntz, D., Fischer, A., Höpp, M., Jacobi, S., Sauer, J., Ohara, T., Sato, T., Shimizu, N., & Schwind, H. (2007) · Ullmann's Encyclopedia of Industrial Chemistry · doi:10.1002/14356007.a01_149.pub2 · Cited by 41 · see citing works
Miyata, S., Liu, B.-F., Shoda, H., Ohara, T., Yamada, H., Suzuki, K., & Kasuga, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4037 · Cited by 37 · see citing works
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Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans
Marrocco, I., Fabio Altieri, F., & Peluso, I. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6501046 · Cited by 874 · see citing works
N-Acetylcysteine as an antioxidant and disulphide breaking agent: the reasons why
Aldini, G., Altomare, A., Baron, G., Vistoli, G., Carini, M., Borsani, L., & Sergio, F. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1468564 · Cited by 837 · see citing works
Self-citationTwarda‐Clapa, A., Olczak, A., Białkowska, A. M., & Koziołkiewicz, M. (2022) · Cells · doi:10.3390/cells11081312 · Cited by 792 · see citing works
Oxidative Stress and Antioxidants in Neurodegenerative Disorders
Olufunmilayo, E. O., Gerke-Duncan, M. B., & Holsinger, R. M. D. (2023) · Antioxidants · doi:10.3390/antiox12020517 · Cited by 722 · see citing works
Sanchez, M. C. C., Lancel, S., Boulanger, É., & Nevière, R. (2018) · Antioxidants · doi:10.3390/antiox7080098 · Cited by 584 · see citing works
Moldogazieva, N. T., Mokhosoev, I. M., Melnikova, T. I., Porozov, Y. B., & Terentiev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3085756 · Cited by 504 · see citing works
Oxidative Stress in Neurodegenerative Diseases: From a Mitochondrial Point of View
Cenini, G., Lloret, A., & Cascella, R. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/2105607 · Cited by 435 · see citing works
Baking, Ageing, Diabetes: A Short History of the Maillard Reaction
Hellwig, M., & Henle, T. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201308808 · Cited by 471 · see citing works
Perrone, A., Giovino, A., Benny, J., & Martinelli, F. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3818196 · Cited by 459 · see citing works
Oxidative Stress and Its Significant Roles in Neurodegenerative Diseases and Cancer
Thanan, R., Oikawa, S., Hiraku, Y., Ohnishi, S., Ma, N., Pinlaor, S., Yongvanit, P., Kawanishi, S., & Murata, M. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms16010193 · Cited by 459 · see citing works
The Impact of Oxidative Stress in Human Pathology: Focus on Gastrointestinal Disorders
Vona, R., Pallotta, L., Cappelletti, M., Severi, C., & Matarrese, P. (2021) · Antioxidants · doi:10.3390/antiox10020201 · Cited by 431 · see citing works
Altered metabolite levels in cancer: implications for tumour biology and cancer therapy
Sullivan, L. B., Gui, D. Y., & Heiden, M. G. V. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.85 · Cited by 406 · see citing works
Mining seed proteome: from protein dynamics to modification profiles
Frolov, A., Мамонтова, Т. В., Ihling, C. H., Lukasheva, E., Bankin, M., Chantseva, V. V., Vikhnina, M., Soboleva, A., Shumilina, J., Mavropolo-Stolyarenko, G., et al. (2018) · Biological Communications · doi:10.21638/spbu03.2018.106 · Cited by 381 · see citing works
Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
“A complete overview of ALE structures with their respective precursors and mechanisms of formation was previously published [50].”
BackgroundToxicity of carbon tetrachloride, free radicals and role of antioxidants
Ünsal, V., Çiçek, M., & Sabancılar, İ. (2020) · Reviews on Environmental Health · doi:10.1515/reveh-2020-0048 · Cited by 336 · see citing works
Rather, J. A., Akhter, N., Ashraf, Q. S., Mir, S. A., Makroo, H. A., Majid, D., Barba, F. J., Khaneghah, A. M., & Dar, B. N. (2022) · Food Packaging and Shelf Life · doi:10.1016/j.fpsl.2022.100945 · Cited by 324 · see citing works
Targeting the Receptor for Advanced Glycation Endproducts (RAGE): A Medicinal Chemistry Perspective
Bongarzone, S., Savickas, V., Luzi, F., & Gee, A. D. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00058 · Cited by 313 · see citing works
Shen, C., Lu, C., Wu, C.-H., Li, K., Kuo, Y., Hsieh, S., & Yu, C. (2020) · Molecules · doi:10.3390/molecules25235591 · Cited by 307 · see citing works
Phospholipids and cholesterol: Inducers of cancer multidrug resistance and therapeutic targets
Kopecka, J., Trouillas, P., Gašparović, A. Č., Gazzano, E., Assaraf, Y. G., & Riganti, C. (2019) · Drug Resistance Updates · doi:10.1016/j.drup.2019.100670 · Cited by 296 · see citing works
Novel advances in shotgun lipidomics for biology and medicine
Wang, M., Wang, C., Han, R. H., & Han, X. (2015) · Progress in Lipid Research · doi:10.1016/j.plipres.2015.12.002 · Cited by 269 · see citing works
A concise appraisal of lipid oxidation and lipoxidation in higher plants
Ramírez, J. D. D. A. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101136 · Cited by 251 · see citing works
Methylglyoxal: An Emerging Signaling Molecule in Plant Abiotic Stress Responses and Tolerance
Hoque, T. S., Hossain, M. A., Mostofa, M. G., Burritt, D. J., Fujita, M., & Tran, L. P. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.01341 · Cited by 247 · see citing works
Uremic Toxicity of Advanced Glycation End Products in CKD
Stinghen, A. E. M., Massy, Z. A., Vlassara, H., Striker, G. E., & Boullier, A. (2015) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014101047 · Cited by 243 · see citing works
Aragno, M., & Mastrocola, R. (2017) · Nutrients · doi:10.3390/nu9040385 · Cited by 239 · see citing works
Oczypok, E. A., Perkins, T. N., & Oury, T. D. (2017) · Paediatric Respiratory Reviews · doi:10.1016/j.prrv.2017.03.012 · Cited by 225 · see citing works
Coffee components and cardiovascular risk: beneficial and detrimental effects
Godos, J., Pluchinotta, F. R., Marventano, S., Buscemi, S., Li Volti, G., Galvano, F., & Grosso, G. (2014) · International Journal of Food Sciences and Nutrition · doi:10.3109/09637486.2014.940287 · Cited by 210 · see citing works
Protein carbonylation: molecular mechanisms, biological implications, and analytical approaches
Akagawa, M. (2020) · Free Radical Research · doi:10.1080/10715762.2020.1851027 · Cited by 209 · see citing works
Redox Signaling and Advanced Glycation Endproducts (AGEs) in Diet-Related Diseases
Cepas, V., Collino, M., Mayo, J. C., & Sainz, R. M. (2020) · Antioxidants · doi:10.3390/antiox9020142 · Cited by 206 · see citing works
Welsh, K. J., Kirkman, M. S., & Sacks, D. B. (2016) · Diabetes Care · doi:10.2337/dc15-2727 · Cited by 205 · see citing works
Brings, S., Fleming, T. H., Freichel, M., Muckenthaler, M. U., Herzig, S., & Nawroth, P. P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18050984 · Cited by 204 · see citing works
tRNA modifications regulate translation during cellular stress
Gu, C., Begley, T. J., & Dedon, P. C. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.09.038 · Cited by 193 · see citing works
Inflammation and Oxidative Stress in Chronic Kidney Disease and Dialysis Patients
Ebert, T., Neytchev, O., Witasp, A., Kublickiene, K. R., Stenvinkel, P., & Shiels, P. G. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8184 · Cited by 190 · see citing works
Protein Oxidation in Aging: Does It Play a Role in Aging Progression?
Reeg, S., & Grune, T. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6062 · Cited by 179 · see citing works
Chen, J.-H., Lin, X., Bu, C., & Zhang, X.-G. (2018) · Nutrition and Metabolism · doi:10.1186/s12986-018-0306-7 · Cited by 154 · see citing works
Advanced Glycation Endproducts in Diabetes and Diabetic Complications
Vlassara, H., & Striker, G. E. (2013) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/j.ecl.2013.07.005 · Cited by 168 · see citing works
Chen, C., Zhang, J., Li, L., Guo, M., He, Y., Dong, Y., Meng, H., & Yi, F. (2022) · Frontiers in Medicine · doi:10.3389/fmed.2022.837222 · Cited by 166 · see citing works
Prevention of Protein Glycation by Natural Compounds
Sadowska‐Bartosz, I., & Bartosz, G. (2015) · Molecules · doi:10.3390/molecules20023309 · Cited by 161 · see citing works
Role of Methylglyoxal in Alzheimer’s Disease
Angeloni, C., Zambonin, L., & Hrelia, S. (2014) · BioMed Research International · doi:10.1155/2014/238485 · Cited by 159 · see citing works
Implication of oxidative stress in progression of diabetic retinopathy
Behl, T., Kaur, I., & Kotwani, A. (2015) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2015.06.001 · Cited by 159 · see citing works
Lipid Peroxidation in Atherosclerotic Cardiovascular Diseases
Gianazza, E., Brioschi, M., Fernandez, A. M., Casalnuovo, F., Altomare, A., Aldini, G., & Banfi, C. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7955 · Cited by 158 · see citing works
Self-citationEffect of diet-derived advanced glycation end products on inflammation
Kellow, N. J., & Coughlan, M. T. (2015) · Nutrition Reviews · doi:10.1093/nutrit/nuv030 · Cited by 154 · see citing works
Analysis of clinical trials on biomaterial and therapeutic applications of chitosan: A review
Kantak, M., & Bharate, S. S. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.118999 · Cited by 154 · see citing works
Lipoxidation in cardiovascular diseases
Gianazza, E., Brioschi, M., Fernandez, A. M., & Banfi, C. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101119 · Cited by 152 · see citing works
MD2 activation by direct AGE interaction drives inflammatory diabetic cardiomyopathy
Wang, Y., Luo, W., Han, J., Khan, Z. A., Fang, Q., Jin, Y., Chen, X., Zhang, Y., Wang, M., Qian, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15978-3 · Cited by 148 · see citing works
Proteomic study of the effect of different cooking methods on protein oxidation in fish fillets
Hu, L., Ren, S., Shen, Q. X., Chen, J., Ye, X., & Ling, J. (2017) · RSC Advances · doi:10.1039/c7ra03408c · Cited by 133 · see citing works
Diet and risk of diabetic retinopathy: a systematic review
Dow, C., Mancini, F. R., Rajaobelina, K., Boutron‐Ruault, M., Balkau, B., Bonnet, F., & Fagherazzi, G. (2017) · European Journal of Epidemiology · doi:10.1007/s10654-017-0338-8 · Cited by 130 · see citing works
Knight, A., Bryan, J., & Murphy, K. J. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.10.005 · Cited by 128 · see citing works
Fossilization transforms vertebrate hard tissue proteins into N-heterocyclic polymers
Wiemann, J., Fabbri, M., Yang, T.-R., Stein, K. H. W., Sander, P. M., Norell, M. A., & Briggs, D. E. G. (2018) · Nature Communications · doi:10.1038/s41467-018-07013-3 · Cited by 128 · see citing works
Bettiga, A., Fiorio, F., Di Marco, F., Trevisani, F., Romani, A., Porrini, E., Salonia, A., Montorsi, F., & Vago, R. (2019) · Nutrients · doi:10.3390/nu11081748 · Cited by 127 · see citing works
Role of advanced glycation end products in carcinogenesis and their therapeutic implications
Schröter, D., & Höhn, A. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190130145549 · Cited by 126 · see citing works
Oxidative theory of atherosclerosis and antioxidants
Salvayre, R., Nègre‐Salvayre, A., & Camaré, C. (2015) · Biochimie · doi:10.1016/j.biochi.2015.12.014 · Cited by 126 · see citing works
The Role of Oxidative Stress in Intervertebral Disc Degeneration
Cao, G., Yang, S., Cao, J., Tan, Z., Wu, L., Dong, F., Ding, W., & Zhang, F. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2166817 · Cited by 126 · see citing works
Collagen Biosynthesis, Processing, and Maturation in Lung Ageing
Onursal, C., Dick, E., Angelidis, I., Schiller, H. B., & Staab-Weijnitz, C. A. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.593874 · Cited by 122 · see citing works
Bhuiyan, M. N. I., Mitsuhashi, S., Sigetomi, K., & Ubukata, M. (2017) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2017.1282805 · Cited by 121 · see citing works
Thakur, S., Jaryal, A., & Bhalla, A. (2024) · Results in Chemistry · doi:10.1016/j.rechem.2024.101350 · Cited by 120 · see citing works
Altomare, A., Baron, G., Gianazza, E., Banfi, C., Carini, M., & Aldini, G. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101899 · Cited by 118 · see citing works
Self-citationRAGE-TLR Crosstalk Sustains Chronic Inflammation in Neurodegeneration
Gąsiorowski, K., Brokos, B., Echeverrı́a, V., Barreto, G. E., & Leszek, J. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0419-4 · Cited by 117 · see citing works
The Advanced Lipoxidation End-Product Malondialdehyde-Lysine in Aging and Longevity
Jové, M., Mota‐Martorell, N., Pradas, I., Martin‐Garí, M., Ayala, V., & Pamplona, R. (2020) · Antioxidants · doi:10.3390/antiox9111132 · Cited by 115 · see citing works
Biomarkers of oxidative and nitro‐oxidative stress: conventional and novel approaches
Gašparović, A. Č., Žarković, N., Žarković, K., Semen, K. O., Kaminskyy, D. V., Yelisyeyeva, O. P., & Bottari, S. P. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13673 · Cited by 115 · see citing works
Sickle Cell Disease: Role of Oxidative Stress and Antioxidant Therapy
Vona, R., Sposi, N. M., Mattia, L., Gambardella, L., Straface, E., & Pietraforte, D. (2021) · Antioxidants · doi:10.3390/antiox10020296 · Cited by 113 · see citing works
Biomonitoring Human Albumin Adducts: The Past, the Present, and the Future
Sabbioni, G., & Turesky, R. J. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00366 · Cited by 108 · see citing works
Zhao, D., Sheng, B., Wu, Y., Li, H., Xu, D., Nian, Y., Mao, S., Li, C., Xu, X., & Zhou, G. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b05891 · Cited by 107 · see citing works
Sadowska‐Bartosz, I., Galiniak, S., & Bartosz, G. (2014) · Molecules · doi:10.3390/molecules191118828 · Cited by 106 · see citing works
Anis, M. A., & Sreerama, Y. N. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.126265 · Cited by 106 · see citing works
Extending the Spectrum of α-Dicarbonyl Compounds in Vivo
Henning, C., Liehr, K., Girndt, M., Ulrich, C., & Glomb, M. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563593 · Cited by 104 · see citing works
The Chemical Reactivity of Membrane Lipids
Duché, G., & Sanderson, J. M. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00608 · Cited by 102 · see citing works
Polyphenols and AGEs/RAGE axis. Trends and challenges
González, I., Morales, M. A., & Armando Rojas, R. (2019) · Food Research International · doi:10.1016/j.foodres.2019.108843 · Cited by 101 · see citing works
Methylglyoxal – An emerging biomarker for diabetes mellitus diagnosis and its detection methods
Ramachandra, B. L., Vedantham, S., Krishnan, U. M., & Rayappan, J. B. B. (2019) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2019.03.010 · Cited by 100 · see citing works
Dual signaling evoked by oxidized LDLs in vascular cells
Nègre‐Salvayre, A., Augè, N., Camaré, C., Bacchetti, T., Ferretti, G., & Salvayre, R. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.006 · Cited by 100 · see citing works
Aldini, G., de Courten, B. V., Regazzoni, L., Gilardoni, E., Ferrario, G., Baron, G., Altomare, A., D’Amato, A., Vistoli, G., & Carini, M. (2020) · Free Radical Research · doi:10.1080/10715762.2020.1856830 · Cited by 99 · see citing works
Self-citationBilova, T. E., Paudel, G., Shilyaev, N., Schmidt, R., Brauch, D., Tarakhovskaya, E., Milrud, S., Николаевна, С. Г., Tissier, A. F., Vogt, T., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.794537 · Cited by 98 · see citing works
The Inflammasome in Chronic Complications of Diabetes and Related Metabolic Disorders
Menini, S., Iacobini, C., Vitale, M., & Pugliese, G. (2020) · Cells · doi:10.3390/cells9081812 · Cited by 97 · see citing works
The onset of lipid peroxidation in rheumatoid arthritis: consequences and monitoring
Łuczaj, W., Gindzienska-Sieskiewicz, E., Jarocka-Karpowicz, I., Andrisic, L., Sierakowski, S., Zarkovic, N., Waeg, G., & Skrzydlewska, E. (2016) · Free Radical Research · doi:10.3109/10715762.2015.1112901 · Cited by 95 · see citing works
Zhu, Z., Huang, M., Cheng, Y., Khan, I. A., & Huang, J. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.01.021 · Cited by 94 · see citing works
Khangholi, S., Majid, F. A. A., Berwary, N. J. A., Ahmad, F., & Aziz, R. (2015) · Planta Medica · doi:10.1055/s-0035-1558086 · Cited by 93 · see citing works
Jiao, L., Stolzenberg‐Solomon, R. Z., Zimmerman, T. P., Duan, Z., Chen, L., Kahle, L., Risch, A., Subar, A. F., Cross, A. J., Hollenbeck, A. R., et al. (2014) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.114.098061 · Cited by 91 · see citing works
Sadowska‐Bartosz, I., Galiniak, S., & Bartosz, G. (2014) · Molecules · doi:10.3390/molecules19044880 · Cited by 91 · see citing works
Kidney, heart and brain: three organs targeted by ageing and glycation
Frimat, M., Daroux, M., Litke, R., Nevière, R., Tessier, F. J., & Boulanger, E. (2017) · Clinical Science · doi:10.1042/cs20160823 · Cited by 88 · see citing works
Dutta, B. J., Singh, S., Seksaria, S., Gupta, G. D., & Singh, A. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106358 · Cited by 87 · see citing works
Oxidative Stress and Its Regulation in Diabetic Retinopathy
Haydinger, C. D., Oliver, G. F., Ashander, L. M., & Smith, J. R. (2023) · Antioxidants · doi:10.3390/antiox12081649 · Cited by 87 · see citing works
Polyunsaturated Fatty Acid Deuteration against Neurodegeneration
Shchepinov, M. S. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.01.010 · Cited by 86 · see citing works
Aging Biomarkers: From Functional Tests to Multi‐Omics Approaches
Kudryashova, K. S., Burka, K., Kulaga, A. Y., Vorobyeva, N. S., & Kennedy, B. K. (2020) · PROTEOMICS · doi:10.1002/pmic.201900408 · Cited by 86 · see citing works
Risk assessment of chemical substances of safety concern generated in processed meats
Flores, M., Mora, L., Reig, M., & Toldrá, F. (2019) · Food Science and Human Wellness · doi:10.1016/j.fshw.2019.07.003 · Cited by 84 · see citing works
The Role of Lipoxidation in the Pathogenesis of Diabetic Retinopathy
Augustine, J., Troendle, E. P., Barabás, P., McAleese, C. A., Friedel, T., Stitt, A. W., & Curtis, T. M. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.621938 · Cited by 83 · see citing works
Hallmarks of Metabolic Reprogramming and Their Role in Viral Pathogenesis
Allen, C. N. S., Arjona, S. P., Santerre, M., & Sawaya, B. E. (2022) · Viruses · doi:10.3390/v14030602 · Cited by 83 · see citing works
The Oxygen Paradox, the French Paradox, and age-related diseases
Davies, J. M. S., Cillard, J., Friguet, B., Cadenas, E., Cadet, J., Cayce, R., Fishmann, A., Liao, D., Bulteau, A.-L., Derbré, F., et al. (2017) · GeroScience · doi:10.1007/s11357-017-0002-y · Cited by 82 · see citing works
Fossil biomolecules reveal an avian metabolism in the ancestral dinosaur
Wiemann, J., Menéndez, I., Crawford, J. M., Fabbri, M., Gauthier, J. A., Hull, P. M., Norell, M. A., & Briggs, D. E. G. (2022) · Nature · doi:10.1038/s41586-022-04770-6 · Cited by 82 · see citing works
Spagnuolo, L., Posta, S. D., Fanali, C., Dugo, L., & Gara, L. D. (2021) · Antioxidants · doi:10.3390/antiox10030424 · Cited by 82 · see citing works
Endogenous Photosensitizers in Human Skin.
Bastos, E., Quina, F., & Baptista, M. S. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00787 · Cited by 69 · see citing works
Using diet-induced obesity to understand a metabolic subtype of osteoarthritis in rats
Collins, K. H., Reimer, R. A., Seerattan, R. A., Leonard, T. R., & Herzog, W. (2015) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2015.01.015 · Cited by 82 · see citing works
Protein lipoxidation: Detection strategies and challenges
Aldini, G., Domingues, M. R., Spickett, C. M., Domingues, P. M., Altomare, A., Sánchez-Gómez, F. J., Oeste, C. L., & Pérez‐Sala, D. (2015) · Redox Biology · doi:10.1016/j.redox.2015.05.003 · Cited by 81 · see citing works
Self-citationMethylglyoxal-Derived Advanced Glycation Endproducts in Multiple Sclerosis
Wetzels, S., Wouters, K., Schalkwijk, C. G., Vanmierlo, T., & Hendriks, J. J. A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020421 · Cited by 80 · see citing works
Dietary Advanced Glycation End Products and Cardiometabolic Risk
Luévano‐Contreras, C., Gómez-Ojeda, A., Macías-Cervantes, M. H., & Garay‐Sevilla, M. E. (2017) · Current Diabetes Reports · doi:10.1007/s11892-017-0891-2 · Cited by 78 · see citing works
Lipoproteins as targets and markers of lipoxidation
Afonso, C. B., & Spickett, C. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.101066 · Cited by 77 · see citing works
Colzani, M., Maddis, D. D., Casali, G., Carini, M., Vistoli, G., & Aldini, G. (2016) · ChemMedChem · doi:10.1002/cmdc.201500552 · Cited by 77 · see citing works
Self-citationPhysiological and therapeutic effects of carnosine on cardiometabolic risk and disease
Baye, E., Ukropcová, B., Ukropec, J., Hipkiss, A. R., Aldini, G., & de Courten, B. V. (2016) · Amino Acids · doi:10.1007/s00726-016-2208-1 · Cited by 77 · see citing works
Self-citationBoozari, M., Soltani, S., & Iranshahi, M. (2019) · Phytotherapy Research · doi:10.1002/ptr.6265 · Cited by 76 · see citing works
Noncalcific Mechanisms of Bioprosthetic Structural Valve Degeneration
Marro, M., Kossar, A. P., Xue, Y., Frasca, A., Levy, R. J., & Ferrari, G. M. (2021) · Journal of the American Heart Association · doi:10.1161/jaha.120.018921 · Cited by 76 · see citing works
Glycation of Plant Proteins: Regulatory Roles and Interplay with Sugar Signalling?
Shumilina, J., Kusnetsova, A., Tsarev, A. A., van Rensburg, H. C. J., Medvedev, S. S., Demidchik, V. V., den Ende, W. V., & Frolov, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092366 · Cited by 75 · see citing works
Mastrocola, R., Nigro, D., Chiazza, F., Medana, C., Bello, F. D., Boccuzzi, G., Collino, M., & Aragno, M. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.022 · Cited by 75 · see citing works
- Authors
- Vistoli, G., De Maddis, D., Cipak, A., Zarkovic, N., Carini, M., & Aldini, G.
- Affiliations
- University of Milan (IT)
- Corresponding author
- Aldini, G.
- Venue
- Free Radical Research
- Publisher
- Informa UK Limited
- Published
- 2013-06-17
- Volume
- 47
- Issue
- sup1
- Pages
- 3-27
- ISSN
- 1029-2470 (ISSN-L)
- 1071-5762
- OpenAlex
- W2136497849
- Cited by
- 823
- References
- 247
- Citations by year
- 2026: 38 · 2025: 58 · 2024: 84 · 2023: 85 · 2022: 96 · 2021: 84 · 2020: 68 · 2019: 69 · 2018: 61 · 2017: 64 · 2016: 41 · 2015: 37 · 2014: 31 · 2013: 3
- FWCI
- 3.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Free Radical Research (publishedVersion)
- PubMed (publishedVersion)
- Institutional Repository of the Ruđer Bošković Institute (Ruđer Bošković Institute) (submittedVersion, other-oa)
- Funders
- Ministero dell'Università e della Ricerca
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- advanced glycation end products, advanced lipoxidation end products, oxidative stress, diabetes mellitus, atherosclerosis, neurological disorders, AGE inhibitors
- MeSH terms
- Receptor for Advanced Glycation End Products, Humans, Pyruvaldehyde, Receptors, Immunologic, Lipid Peroxidation, Maillard Reaction, Glycation End Products, Advanced, Protein Carbonylation
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